Structural Bases for Substrate and Inhibitor Recognition by Matrix Metalloproteinases

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Abstract:

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases which are involved in the proteolytic processing of several components of the extracellular matrix. As a consequence, MMPs are implicated in several physiological and pathological processes, like skeletal growth and remodelling, wound healing, cancer, arthritis, and multiple sclerosis, raising a very widespread interest toward this class of enzymes as potential therapeutic targets. Here, structure-function relationships are discussed to highlight the role of different MMP domains on substrate/inhibitor recognition and processing and to attempt the formulation of advanced guidelines, based on natural substrates, for the design of inhibitors more efficient in vivo.

Keywords: Enzyme-inhibitor recognition; Enzyme-substrate recognition; Matrix metalloproteinases; Structural bases

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986708785747490

Affiliations: Colosseum Combinatorial Chemistry Centre for Technology (C4T S.C.a r.l.), Via della Ricerca Scientifica s.n.c, I-00133 Roma, Italy.

Publication date: September 1, 2008

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.

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